| Tag | Content |
|---|
| CPLM ID | CPLM-014488 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Protein disulfide-isomerase A6 |
Protein Synonyms/Alias | Calcium-binding protein 1; CaBP1; Protein disulfide isomerase P5; Thioredoxin domain-containing protein 7 |
Gene Name | Pdia6 |
Gene Synonyms/Alias | Cabp1; Txndc7 |
Created Date | July 27, 2013 |
Organism | Rattus norvegicus (Rat) |
NCBI Taxa ID | 10116 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 67 | RLTPEWKKAASALKD | acetylation | [1] | | 160 | RGDSSSKKDVVELTD | acetylation | [1] | | 366 | MAAINARKMKFALLK | acetylation | [1] |
|
Reference | [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns. Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV. Cell Rep. 2012 Aug 30;2(2):419-31. [ PMID: 22902405] |
Functional Description | May function as a chaperone that inhibits aggregation of misfolded proteins. Plays a role in platelet aggregation and activation by agonists such as convulxin, collagen and thrombin (By similarity). |
Sequence Annotation | DOMAIN 21 133 Thioredoxin 1.
DOMAIN 151 287 Thioredoxin 2.
MOTIF 437 440 Prevents secretion from ER (By
ACT_SITE 55 55 Nucleophile (By similarity).
ACT_SITE 58 58 Nucleophile (By similarity).
ACT_SITE 190 190 Nucleophile (By similarity).
ACT_SITE 193 193 Nucleophile (By similarity).
MOD_RES 428 428 Phosphoserine (By similarity).
DISULFID 55 58 Redox-active (By similarity).
DISULFID 190 193 Redox-active (By similarity). |
Keyword | Calcium; Cell membrane; Chaperone; Complete proteome; Direct protein sequencing; Disulfide bond; Endoplasmic reticulum; Isomerase; Membrane; Phosphoprotein; Redox-active center; Reference proteome; Repeat; Signal. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 440 AA |
Protein Sequence | MARLVLGLVS CTFFLAVSAL YSSSDDVIEL TPSNFNREVI QSDSLWLVEF YAPWCGHCQR 60
LTPEWKKAAS ALKDVVKVGA VNADKHQSLG GQYGVQGFPT IKIFGANKNK PEDYQGGRTG 120
EAIVDAALSA LRQLVKDRLG GRSGGYSSGK QGRGDSSSKK DVVELTDDTF DKNVLDSEDV 180
WMVEFYAPWC GHCKNLEPEW AAAATEVKEQ TKGKVKLAAV DATVNQVLAS RYGIKGFPTI 240
KIFQKGESPV DYDGGRTRSD IVSRALDLFS DNAPPPELLE IINEDIAKKT CEEHQLCVVA 300
VLPHILDTGA TGRNSYLEVL LKLADKYKKK MWGWLWTEAG AQYELENALG IGGFGYPAMA 360
AINARKMKFA LLKGSFSEQG INEFLRELSF GRGSTAPVGG GSFPNITPRE PWDGKDGELP 420
VEDDIDLSDV ELDDLEKDEL 440 |
Gene Ontology | GO:0005788; C:endoplasmic reticulum lumen; IDA:HGNC. GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; TAS:RGD. GO:0042470; C:melanosome; ISS:UniProtKB. GO:0005886; C:plasma membrane; ISS:UniProtKB. GO:0005509; F:calcium ion binding; TAS:RGD. GO:0009055; F:electron carrier activity; IEA:InterPro. GO:0003756; F:protein disulfide isomerase activity; ISS:UniProtKB. GO:0015035; F:protein disulfide oxidoreductase activity; IEA:InterPro. GO:0045454; P:cell redox homeostasis; IEA:InterPro. GO:0006662; P:glycerol ether metabolic process; IEA:InterPro. GO:0070527; P:platelet aggregation; ISS:UniProtKB. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |